GenomeNet

Database: UniProt
Entry: A0A444X277_ARAHY
LinkDB: A0A444X277_ARAHY
Original site: A0A444X277_ARAHY 
ID   A0A444X277_ARAHY        Unreviewed;       341 AA.
AC   A0A444X277;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=S1 motif domain-containing protein {ECO:0000259|PROSITE:PS50126};
GN   ORFNames=Ahy_B10g102496 {ECO:0000313|EMBL:RYQ83703.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ83703.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYQ83703.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYQ83703.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC       {ECO:0000256|ARBA:ARBA00007223}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RYQ83703.1}.
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DR   EMBL; SDMP01000020; RYQ83703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A444X277; -.
DR   STRING; 3818.A0A444X277; -.
DR   OrthoDB; 4371132at2759; -.
DR   Proteomes; UP000289738; Chromosome b10.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd04452; S1_IF2_alpha; 1.
DR   Gene3D; 3.30.70.1130; EIF_2_alpha; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR044126; S1_IF2_alpha.
DR   InterPro; IPR024055; TIF2_asu_C.
DR   InterPro; IPR024054; TIF2_asu_middle_sf.
DR   InterPro; IPR011488; TIF_2_asu.
DR   PANTHER; PTHR10602; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR   PANTHER; PTHR10602:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR   Pfam; PF07541; EIF_2_alpha; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF110993; eIF-2-alpha, C-terminal domain; 1.
DR   SUPFAM; SSF116742; eIF2alpha middle domain-like; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT   DOMAIN          18..89
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          300..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..329
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  38605 MW;  1BD5F705F9350237 CRC64;
     MGPNLECRMY EAKYPEVDMA VMIQVKNIAD MGAYVSLLEY NNIEGMILFS ELSRRRIRSV
     SSLIKVGRIE PVMVLRVDKD KGYIDLSKRR VSEEDIQACE ERYNKSKLVH SIMRHVAETL
     NIDLEELYVH IGWPLYRKYG HAFEAFKIIV TDPDSVLNAL TREIKEAGPD GQEVTKVVPA
     VTEEVKDSLV KNIRRRMTPQ PLKIRADIEM KCFQFDGVLH IKEAMRKAEA AGNDDCPVKI
     KLVAPPLYVL TTQTLDKEQG IQVLNNAITS CTESIEQHKG KLVVKEAPRA VSERDDKLLA
     EHMAKLRQDN EEVSGDEDSE EEEDTGMGDV DLDNNGTGIT E
//
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